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Article

The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.

International journal of molecular sciences - 16 Mar 2018

Rhoads Shannon N, Monahan Zachary T, Yee Debra S, Shewmaker Frank P

Abstract excerpt

Subcellular mislocalization and aggregation of the human FUS protein occurs in neurons of patients with subtypes of amyotrophic lateral sclerosis and frontotemporal dementia. FUS is one of several RNA-binding proteins that can functionally self-associate into distinct liquid-phase droplet structures. It is postulated that aberrant interactions within the dense phase-separated state can potentiate FUS's transition...

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Share to Amyotrophic Lateral Sclerosis
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Open in PubMed Open full text

Identifiers

PMID: 29547565
DOI: 10.3390/ijms19030886
PMCID: PMC5877747

Genes

FUS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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